Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein-Protein Interfaces02:04

Protein-Protein Interfaces

4.4K
4.4K
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.4K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.4K
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

63.0K
Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
63.0K
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

19.2K
19.2K
Conjugated Proteins02:50

Conjugated Proteins

27.2K
Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...
27.2K
Conserved Binding Sites01:49

Conserved Binding Sites

5.0K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
5.0K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Affective Forecasting and Memory Biases during the Tokyo and Beijing Olympics.

Affective science·2026
Same author

Impact of Nucleotide Flexibility on Aptamer-Protein Recognition: RNA vs RNA-DNA Chimera.

ACS chemical biology·2026
Same author

Instability of cooperation based on fictitious belief: an experiment with artificial supernatural punishment.

Scientific reports·2026
Same author

<i>In Silico</i> Discovery of SARS-CoV-2 Main Protease Inhibitors Using Docking, Molecular Dynamics, and Fragment Molecular Orbital Calculations.

The journal of physical chemistry. B·2025
Same author

A facile access to aliphatic trifluoromethyl ketones <i>via</i> photocatalyzed cross-coupling of bromotrifluoroacetone and alkenes.

Organic & biomolecular chemistry·2024
Same author

Nucleophilic fluorine substitution reaction of α-carbonyl benzyl bromide, phenylthiofluoroalkyl bromide, and 2-bromo-2-phenoxyacetonitrile.

RSC advances·2024

Related Experiment Video

Updated: Jan 8, 2026

Engineering Antiviral Agents via Surface Plasmon Resonance
13:00

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

2.7K

Visualization of interfacial electrostatic complementarity reveals evolutionary changes in SARS-CoV-2 RBD-hACE2

Yosuke Muroya1, Hiroki Ozono1, Takeshi Ishikawa1

  • 1Department of Chemistry, Biotechnology, and Chemical Engineering, Graduate School of Science and Engineering, Kagoshima University, 1-21-40 Korimoto, Kagoshima, Kagoshima 890-0065, Japan. ishi@cb.kagoshima-u.ac.jp.

Physical Chemistry Chemical Physics : PCCP
|December 15, 2025
PubMed
Summary

Understanding mutations in the SARS-CoV-2 spike protein's receptor-binding domain (RBD) is key. A new method, VIINEC, visualizes electrostatic changes in RBD-hACE2 interactions, revealing adaptive mechanisms in the human ACE2 protein during viral evolution.

More Related Videos

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
10:50

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

Published on: September 15, 2010

9.9K
Advancing High-Resolution Imaging of Virus Assemblies in Liquid and Ice
08:31

Advancing High-Resolution Imaging of Virus Assemblies in Liquid and Ice

Published on: July 20, 2022

3.6K

Related Experiment Videos

Last Updated: Jan 8, 2026

Engineering Antiviral Agents via Surface Plasmon Resonance
13:00

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

2.7K
Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
10:50

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

Published on: September 15, 2010

9.9K
Advancing High-Resolution Imaging of Virus Assemblies in Liquid and Ice
08:31

Advancing High-Resolution Imaging of Virus Assemblies in Liquid and Ice

Published on: July 20, 2022

3.6K

Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • The SARS-CoV-2 spike protein's receptor-binding domain (RBD) interacts with human angiotensin-converting enzyme 2 (hACE2), a critical step in viral infection.
  • Amino acid mutations within the RBD drive viral evolution and can alter this crucial protein-protein interaction (PPI).

Purpose of the Study:

  • To comprehensively analyze the impact of amino acid mutations in the SARS-CoV-2 RBD on the RBD-hACE2 PPI.
  • To investigate the adaptive changes in electrostatic complementarity at the RBD-hACE2 interface during viral evolution.

Main Methods:

  • Utilized a novel PPI analysis method, visualization of interfacial electrostatic complementarity (VIINEC).
  • Applied VIINEC to study RBD-hACE2 complexes across 15 SARS-CoV-2 variants.
  • Visualized and analyzed electrostatic potential (ESP) at the protein-protein interface.

Main Results:

  • Observed significant alterations in the electrostatic potential (ESP) of RBDs across different SARS-CoV-2 variants.
  • Demonstrated that the hACE2 protein's ESP significantly changed in response to RBD mutations, despite having no mutations itself.
  • Found that hACE2 maintained high electrostatic complementarity with evolving RBDs.
  • Attributed adaptive ESP changes in hACE2 to conformational shifts in four charged residues.

Conclusions:

  • VIINEC provides an intuitive method for understanding how mutations affect PPIs by visualizing electrostatic complementarity.
  • SARS-CoV-2 variants exhibit adaptive changes in the RBD-hACE2 interface, with hACE2 dynamically adjusting its electrostatic profile.
  • These findings highlight the complex co-evolutionary dynamics between the virus and its host receptor.